[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=New Zealand white; TISSUE=Liver; DOI=10.1021/bi00372a008; PubMed=3026463 [NCBI, ExPASy, EBI, Israel, Japan] Hu S.-I., Miller S.M., Samols D.; "Cloning and characterization of the gene for rabbit C-reactive protein."; Biochemistry 25:7834-7839(1986).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3007506 [NCBI, ExPASy, EBI, Israel, Japan] Syin C., Gotschlich E.C., Liu T.-Y.; "Rabbit C-reactive protein. Biosynthesis and characterization of cDNA clones."; J. Biol. Chem. 261:5473-5479(1986).
[3]	PROTEIN SEQUENCE OF 21-225. PubMed=6754715 [NCBI, ExPASy, EBI, Israel, Japan] Wang C.-M., Nguyen N.Y., Yonaha K., Robey F., Liu T.-Y.; "Primary structure of rabbit C-reactive protein."; J. Biol. Chem. 257:13610-13615(1982).

Comments

FUNCTION: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells (By similarity).
COFACTOR: Binds 2 calcium ions per subunit (By similarity).
SUBUNIT: Homopentamer. Pentaxin (or pentraxin) have a discoid arrangement of 5 non-covalently bound subunits (By similarity).
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Found in plasma.
INDUCTION: The concentration of CRP in plasma increases greatly during acute phase response to tissue injury, infection or other inflammatory stimuli.
MISCELLANEOUS: Asp-61, Arg-76, Arg-77, and Glu-81 may be involved in the calcium-dependent binding of phosphorylcholine, a property that may be important for the biological function of this protein.
SIMILARITY: Belongs to the pentaxin family.
SIMILARITY: Contains 1 pentaxin domain.
WEB RESOURCE: Name=Protein Spotlight; Note=No more Christmas pudding? - Issue 30 of January 2003; URL="http://www.expasy.org/spotlight/back_issues/sptlt030.shtml";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M14538; AAA75403.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L47237; AAA75404.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M13497; AAA31206.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A25605; CJRB.

NP_001075734.1; -.

3D structure databases

HSSP

P02741; 1LJ7. [HSSP ENTRY / PDB]

SMR

P02742; 20-225.

ModBase

P02742.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006953;	Biological process: acute-phase response (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013320; ConA_like_subgrp.
IPR001759; Pentaxin.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.120.200; ConA_like_subgrp; 1.

Pfam

PF00354; Pentaxin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00895; PENTAXIN.

ProDom

PD002153; Pentaxin; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00159; PTX; 1.
SMART graphical view of domain structure.

PROSITE

PS00289; PENTAXIN; 1.

Genome annotation databases

Ensembl

ENSOCUG00000004702; Oryctolagus cuniculus. [Contig view]

GeneID

100009091; -.

Phylogenomic databases

HOVERGEN

P02742; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acute phase; Calcium; Direct protein sequencing; Metal-binding; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`
`CHAIN`	`21 225`	`205`	`C-reactive protein.`	`PRO_0000023531`
`DOMAIN`	`21 225`	`205`	`Pentaxin.`
`METAL`	`80 80`		`Calcium 1 (By similarity).`
`METAL`	`158 158`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`159 159`		`Calcium 1 (By similarity).`
`METAL`	`159 159`		`Calcium 2 (By similarity).`
`METAL`	`169 169`		`Calcium 2 (By similarity).`
`DISULFID`	`55 116`
`VARIANT`	`62 62`	`1`	`L -> K.`
`VARIANT`	`89 89`	`1`	`D -> V.`
`CONFLICT`	`10 10`		`T -> I (in Ref. 2; AAA31206).`
`CONFLICT`	`46 46`		`K -> T (in Ref. 3; AA sequence).`
`CONFLICT`	`50 50`		`K -> L (in Ref. 3; AA sequence).`
`CONFLICT`	`76 76`		`R -> K (in Ref. 1; AAA75404).`
`CONFLICT`	`84 88`		`LFWSK -> FFVKE (in Ref. 3; AA sequence).`
`CONFLICT`	`91 91`		`G -> V (in Ref. 3; AA sequence).`
`CONFLICT`	`93 101`		`Missing (in Ref. 3; AA sequence).`
`CONFLICT`	`108 108`		`I -> V (in Ref. 2; AAA31206).`
`CONFLICT`	`167 167`		`K -> W (in Ref. 3; AA sequence).`
`CONFLICT`	`177 177`		`N -> D (in Ref. 3; AA sequence).`
`CONFLICT`	`193 193`		`I -> V (in Ref. 3; AAA31206).`

Sequence information

Length: 225 AA [This is the length of the unprocessed precursor]

Molecular weight: 25493 Da [This is the MW of the unprocessed precursor]

CRC64: C6D634FDE844438F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKLLWCFLT LVSFSNMSDQ AGMHKKAFVF PKESDNSYVS LNAQLKKPLK AFTVCLYFYT 

        70         80         90        100        110        120 
DLSMTRGYSI FSYATRRQFN EILLFWSKDI GYSFSVGGDE IIFKVSDIPV DPTHLCASWE 

       130        140        150        160        170        180 
SSTGIAELWV DGKPMVRKSL KKGYILGPEA SIILGQDQDS FGGSFEKQQS LVGDIGNVNM 

       190        200        210        220 
WDYALSPEEI NTIYAGGTFS PNVLDWRELT YQVRGEVHVK PQLWP

P02742 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools